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Identification of MyoD Interactome Using Tandem Affinity Purification Coupled to Mass Spectrometry

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DHPR alpha1S subunit controls skeletal muscle mass and morphogenesis.

France Piétri-Rouxel¹, Christel Gentil, Stéphane Vassilopoulos

¹UMR 7215, CNRS, UMR S 974 Inserm, Institut de Myologie, Université Pierre et Marie Curie, Paris, France. france.pietri-rouxel@upmc.fr

The EMBO Journal

|December 25, 2009

Summary

Downregulating the alpha1S subunit in skeletal muscle caused atrophy via autophagy, revealing a sarcolemmal alpha1S fraction that senses muscle activity.

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Myo-mechanical Analysis of Isolated Skeletal Muscle

Myo-mechanical Analysis of Isolated Skeletal Muscle

Published on: February 22, 2011

Area of Science:

Muscle physiology
Cellular signaling
Molecular biology

Background:

The alpha1S subunit in skeletal muscle has a dual role, forming L-type Ca(2+) channels and acting as a voltage sensor for excitation-contraction coupling.
It has been hypothesized that L-type Ca(2+) channels may also function as voltage-gated sensors influencing transcriptional activity and differentiation.

Purpose of the Study:

To investigate the function of the alpha1S subunit in adult skeletal muscle.
To explore the role of a specific sarcolemmal alpha1S fraction in muscle signaling.

Main Methods:

Utilized the U7-exon skipping strategy for sustained alpha1S downregulation in adult skeletal muscle.
Analyzed muscle atrophy, autophagy pathway activation, and alpha1S localization using subcellular investigations.

Main Results:

Long-lasting alpha1S downregulation induced massive muscle atrophy without paralysis, despite residual alpha1S in the tubular system.
Atrophy was linked to autophagy pathway activation, involving neuronal nitric oxide synthase, FoxO3A, and autophagy-related genes.
Disappearance of a minor sarcolemmal alpha1S fraction correlated with muscle atrophy.

Conclusions:

A specific sarcolemmal alpha1S fraction plays a crucial role in regulating muscle anabolic/catabolic state.
This sarcolemmal alpha1S fraction may function as a molecular sensor of muscle activity, impacting cellular signaling pathways.